Analytical Data
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Gene name
phrB
- Application
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Alternative Names
DNA photolyase Photoreactivating enzyme
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00914
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Expression Region
1-472aa
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Molecular Weight
73.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of the PhrB protein, a key component in the regulatory mechanisms of bacterial communication, has gained significant attention in recent years. PhrB, or pleiotropic regulatory protein B, is primarily known for its role in quorum sensing, a process by which bacteria coordinate their behavior based on population density. This protein is particularly important in the context of *Bacillus subtilis*, a model organism for studying bacterial physiology. Research has shown that PhrB influences biofilm formation, sporulation, and the production of various exoenzymes, thereby impacting the development and survival strategies of the bacterial community. Furthermore, understanding PhrB's structure and function can provide insights into its interaction with other regulatory proteins, enabling the design of novel antimicrobial strategies that target bacterial communication pathways. Recombinant DNA technology has facilitated the production of PhrB in heterologous systems, allowing for detailed biochemical and structural analyses. This research not only uncovers the intricate networks of bacterial signaling but also addresses broader implications for infectious disease management and biotechnology applications. As such, the characterization of PhrB and its associated pathways represents a frontier in microbiological research, with the potential to revolutionize our approach to bacterial infections and microbial ecology.
